Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization

BACKGROUND: Polybasic helical peptides, such as peptide p5, bind human amyloid extracts and synthetic amyloid fibrils. When radiolabeled, peptide p5 has been shown to specifically bind amyloid in vivo thereby allowing imaging of the disease. Structural requirements for heparin and amyloid binding ha...

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Dettagli Bibliografici
Pubblicato in:Biochem Biophys Rep
Autori principali: Wall, Jonathan S., Williams, Angela, Wooliver, Craig, Martin, Emily B., Cheng, Xiaolin, Heidel, R. Eric, Kennel, Stephen J.
Natura: Artigo
Lingua:Inglês
Pubblicazione: Elsevier 2016
Soggetti:
Research Article
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC5363963/
https://ncbi.nlm.nih.gov/pubmed/28345062
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbrep.2016.08.007
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